Gomi H, Ikeda T, Kunieda T, Itohara S, Prusiner S B, Yamanouchi K
Institute for Virus Research, Kyoto University, Japan.
Neurosci Lett. 1994 Jan 31;166(2):171-4. doi: 10.1016/0304-3940(94)90478-2.
In order to elucidate the relationship between the prion protein (PrP) structure and the development of spongiform encephalopathy in zitter rats, we analyzed the nucleotide sequences and restriction fragment length variation (RFLV) of the Prn gene encoding PrP in zitter rats and inbred SD/J rats as a control. Prn genes from two strains had identical nucleotide sequences in their coding sequences. Obvious RFLV on the locus was not detected in zitter rats by a Southern blot hybridization. Consistently, zitter rat brains express the normal cellular PrP (PrPC), but do not accumulate the protease-resistant modified isoform (PrPSC). These results indicate that PrP is not involved in the pathogenesis of spongiform encephalopathy in zitter rats.
为了阐明颤抖大鼠中朊病毒蛋白（PrP）结构与海绵状脑病发展之间的关系，我们分析了颤抖大鼠和作为对照的近交系SD/J大鼠中编码PrP的Prn基因的核苷酸序列和限制性片段长度变异（RFLV）。两个品系的Prn基因在其编码序列中具有相同的核苷酸序列。通过Southern印迹杂交在颤抖大鼠中未检测到该位点上明显的RFLV。一致地，颤抖大鼠脑表达正常的细胞型PrP（PrPC），但不积累抗蛋白酶的修饰异构体（PrPSC）。这些结果表明PrP不参与颤抖大鼠海绵状脑病的发病机制。
